Adsorption of Fibrinogen on Silica Surfaces-The Effect of Attached Nanoparticles
(2020) In Biomolecules 10(3).- Abstract
When a biomaterial is inserted into the body, proteins rapidly adsorb onto its surface, creating a conditioning protein film that functions as a link between the implant and adhering cells. Depending on the nano-roughness of the surface, proteins will adsorb in different amounts, with different conformations and orientations, possibly affecting the subsequent attachment of cells to the surface. Thus, modifications of the surface nanotopography of an implant may prevent biomaterial-associated infections. Fibrinogen is of particular importance since it contains adhesion epitopes that are recognized by both eukaryotic and prokaryotic cells, and can therefore influence the adhesion of bacteria. The aim of this study was to model adsorption... (More)
When a biomaterial is inserted into the body, proteins rapidly adsorb onto its surface, creating a conditioning protein film that functions as a link between the implant and adhering cells. Depending on the nano-roughness of the surface, proteins will adsorb in different amounts, with different conformations and orientations, possibly affecting the subsequent attachment of cells to the surface. Thus, modifications of the surface nanotopography of an implant may prevent biomaterial-associated infections. Fibrinogen is of particular importance since it contains adhesion epitopes that are recognized by both eukaryotic and prokaryotic cells, and can therefore influence the adhesion of bacteria. The aim of this study was to model adsorption of fibrinogen to smooth or nanostructured silica surfaces in an attempt to further understand how surface nanotopography may affect the orientation of the adsorbed fibrinogen molecule. We used a coarse-grained model, where the main body of fibrinogen (visible in the crystal structure) was modeled as rigid and the flexible α C-chains (not visible in the crystal structure) were modeled as completely disordered. We found that the elongated fibrinogen molecule preferably adsorbs in such a way that it protrudes further into solution on a nanostructured surface compared to a flat one. This implicates that the orientation on the flat surface increases its bio-availability.
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- author
- Hyltegren, Kristin LU ; Hulander, Mats ; Andersson, Martin and Skepö, Marie LU
- organization
- publishing date
- 2020-03-06
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- coarse-grained modeling, fibrinogen, nanoparticles, nanotopography, protein adsorption
- in
- Biomolecules
- volume
- 10
- issue
- 3
- article number
- 413
- publisher
- MDPI AG
- external identifiers
-
- pmid:32155964
- scopus:85081694567
- ISSN
- 2218-273X
- DOI
- 10.3390/biom10030413
- language
- English
- LU publication?
- yes
- id
- 1893d730-b502-4eb5-8408-346b96d9bd12
- date added to LUP
- 2020-04-01 15:19:21
- date last changed
- 2024-05-01 07:34:26
@article{1893d730-b502-4eb5-8408-346b96d9bd12,
abstract = {{<p>When a biomaterial is inserted into the body, proteins rapidly adsorb onto its surface, creating a conditioning protein film that functions as a link between the implant and adhering cells. Depending on the nano-roughness of the surface, proteins will adsorb in different amounts, with different conformations and orientations, possibly affecting the subsequent attachment of cells to the surface. Thus, modifications of the surface nanotopography of an implant may prevent biomaterial-associated infections. Fibrinogen is of particular importance since it contains adhesion epitopes that are recognized by both eukaryotic and prokaryotic cells, and can therefore influence the adhesion of bacteria. The aim of this study was to model adsorption of fibrinogen to smooth or nanostructured silica surfaces in an attempt to further understand how surface nanotopography may affect the orientation of the adsorbed fibrinogen molecule. We used a coarse-grained model, where the main body of fibrinogen (visible in the crystal structure) was modeled as rigid and the flexible α C-chains (not visible in the crystal structure) were modeled as completely disordered. We found that the elongated fibrinogen molecule preferably adsorbs in such a way that it protrudes further into solution on a nanostructured surface compared to a flat one. This implicates that the orientation on the flat surface increases its bio-availability.</p>}},
author = {{Hyltegren, Kristin and Hulander, Mats and Andersson, Martin and Skepö, Marie}},
issn = {{2218-273X}},
keywords = {{coarse-grained modeling; fibrinogen; nanoparticles; nanotopography; protein adsorption}},
language = {{eng}},
month = {{03}},
number = {{3}},
publisher = {{MDPI AG}},
series = {{Biomolecules}},
title = {{Adsorption of Fibrinogen on Silica Surfaces-The Effect of Attached Nanoparticles}},
url = {{http://dx.doi.org/10.3390/biom10030413}},
doi = {{10.3390/biom10030413}},
volume = {{10}},
year = {{2020}},
}